4.7 Article

The role of positive charged residue in the proton-transfer mechanism of two-domain laccase from Streptomyces griseoflavus Ac-993

期刊

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
卷 40, 期 18, 页码 8324-8331

出版社

TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2021.1911852

关键词

Two-domain laccases; crystal structures; T2; T3 copper site; tunnels; proton transfer

资金

  1. Russian Foundation for Basic Research [18-04-00270a, 19-34-90121]
  2. Fundacao para a Ciencia e a Tecnologia (FCT) [IF/00256/2015]

向作者/读者索取更多资源

This study investigated the role of the Arg240 residue in the two-domain laccase from Streptomyces griseoflavus Ac-993, with X-ray structural analysis and kinetic characterization of two mutants providing support for the involvement of this residue in protonation events during the reductive cleavage of dioxygen to water.
Multi-copper oxidases are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. This process takes place at the trinuclear copper center of the enzymes. Previously, the main catalytic stages for three-domain (3D) laccases have been identified. However, for bacterial small two-domain (2D) laccases several questions remain to be answered. One of them is the nature of the protonation events upon the reductive cleavage of dioxygen to water. In 3D laccases, acidic residues play a key role in the protonation mechanisms. In this study, the role of the Arg240 residue, located within the T2 tunnel of 2D laccase from Streptomyces griseoflavus Ac-993, was investigated. X-ray structural analysis and kinetic characterization of two mutants, R240A and R240H, have provided support for a role of this residue in the protonation events. Communicated by Ramaswamy H. Sarma

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